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MARK3

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

MARK3

Available structures

PDB

Ortholog search:PDBe RCSB

List of PDB id codes
2QNJ,3FE3

Identifiers

Aliases

MARK3, CTAK1, KP78, PAR1A, Par-1a, microtubule affinity regulating kinase 3, VIPB

External IDs

OMIM:602678;MGI:1341865;HomoloGene:55653;GeneCards:MARK3;OMA:MARK3 - orthologs

Gene location (Human)

Chr.	Chromosome 14 (human)^[1]

Band	14q32.32-q32.33	Start	103,385,377bp^[1]
Band	14q32.32-q32.33	End	103,503,831bp^[1]

Gene location (Mouse)

Chr.	Chromosome 12 (mouse)^[2]

Band	12\|12 F1	Start	111,540,957bp^[2]
Band	12\|12 F1	End	111,622,655bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

cerebellar hemisphere

right hemisphere of cerebellum

body of pancreas

apex of heart

right adrenal cortex

left uterine tube

right lung

right auricle

left adrenal gland

left adrenal cortex

Top expressed in

genital tubercle

tail of embryo

ventricular zone

spermatid

molar

right kidney

proximal tubule

Gonadal ridge

otic vesicle

ganglionic eminence

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	transferase activity nucleotide binding protein kinase activity kinase activity protein binding ATP binding protein serine/threonine kinase activity tau protein binding tau-protein kinase activity
Cellular component	cytosol membrane extracellular exosome plasma membrane cytoplasm dendrite cell projection
Biological process	phosphorylation MAPK cascade protein phosphorylation microtubule cytoskeleton organization establishment of cell polarity negative regulation of hippo signaling peptidyl-serine phosphorylation positive regulation of protein binding intracellular signal transduction peptidyl-serine autophosphorylation
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


4140


17169

Ensembl


ENSG00000075413


ENSMUSG00000007411

UniProt


P27448


Q03141

RefSeq (mRNA)


NM_001128918 NM_001128919 NM_001128920 NM_001128921 NM_002376


NM_021516 NM_022801 NM_001370744 NM_001370745

RefSeq (protein)


NP_001122390 NP_001122391 NP_001122392 NP_001122393 NP_002367


NP_067491 NP_073712 NP_001357673 NP_001357674

Location (UCSC)

Chr 14: 103.39 – 103.5 Mb

Chr 12: 111.54 – 111.62 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

MAP/microtubule affinity-regulating kinase 3 is anenzyme that in humans is encoded by theMARK3gene.^[5]^[6]

Interactions

[edit]

MARK3 has been shown tointeract withStratifin.^[7]^[8]

It has been linked to a form of genetic blindness, believed to be a genetic recessive disease that progressively destroys the eyes.^[9]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000075413 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000007411 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^Ono T, Kawabe T, Sonta S, Okamoto T (April 1998). "Assignment of MARK3 alias KP78 to human chromosome band 14q32.3 by in situ hybridization".Cytogenet Cell Genet.79 (1–2):101–2.doi:10.1159/000134692.PMID 9533022.
^"Entrez Gene: MARK3 MAP/microtubule affinity-regulating kinase 3".
^Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein–protein interaction network".Nature.437 (7062):1173–8.Bibcode:2005Natur.437.1173R.doi:10.1038/nature04209.PMID 16189514.S2CID 4427026.
^Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (June 2005)."Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer".Mol. Cell. Proteomics.4 (6):785–95.doi:10.1074/mcp.M500021-MCP200.PMID 15778465.
^"Découverte d'un gène provoquant une cécité - Communiqués de presse - UNIGE". 23 July 2018.

Tassan JP, Le Goff X (2004)."An overview of the KIN1/PAR-1/MARK kinase family".Biol. Cell.96 (3):193–9.doi:10.1016/j.biolcel.2003.10.009.PMID 15182702.
Meller N, Liu YC, Collins TL, Bonnefoy-Bérard N, Baier G, Isakov N, Altman A (1996)."Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function".Mol. Cell. Biol.16 (10):5782–91.doi:10.1128/MCB.16.10.5782.PMC 231579.PMID 8816492.
Peng CY, Graves PR, Ogg S, Thoma RS, Byrnes MJ, Wu Z, Stephenson MT, Piwnica-Worms H (1998). "C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and promotes 14-3-3 protein binding".Cell Growth Differ.9 (3):197–208.PMID 9543386.
Sun TQ, Lu B, Feng JJ, Reinhard C, Jan YN, Fantl WJ, Williams LT (2001). "PAR-1 is a Dishevelled-associated kinase and a positive regulator of Wnt signalling".Nat. Cell Biol.3 (7):628–36.doi:10.1038/35083016.PMID 11433294.S2CID 1128604.
Spicer J, Rayter S, Young N, Elliott R, Ashworth A, Smith D (2003). "Regulation of the Wnt signalling component PAR1A by the Peutz-Jeghers syndrome kinase LKB1".Oncogene.22 (30):4752–6.doi:10.1038/sj.onc.1206669.PMID 12879020.S2CID 9945293.
Müller J, Ritt DA, Copeland TD, Morrison DK (2003)."Functional analysis of C-TAK1 substrate binding and identification of PKP2 as a new C-TAK1 substrate".EMBO J.22 (17):4431–42.doi:10.1093/emboj/cdg426.PMC 202368.PMID 12941695.
Trinczek B, Brajenovic M, Ebneth A, Drewes G (2004)."MARK4 is a novel microtubule-associated proteins/microtubule affinity-regulating kinase that binds to the cellular microtubule network and to centrosomes".J. Biol. Chem.279 (7):5915–23.doi:10.1074/jbc.M304528200.PMID 14594945.
Navarro-Lérida I, Martínez Moreno M, Roncal F, Gavilanes F, Albar JP, Rodríguez-Crespo I (2004). "Proteomic identification of brain proteins that interact with dynein light chain LC8".Proteomics.4 (2):339–46.doi:10.1002/pmic.200300528.PMID 14760703.S2CID 8868600.
Bachmann M, Hennemann H, Xing PX, Hoffmann I, Möröy T (2005)."The oncogenic serine/threonine kinase Pim-1 phosphorylates and inhibits the activity of Cdc25C-associated kinase 1 (C-TAK1): a novel role for Pim-1 at the G2/M cell cycle checkpoint".J. Biol. Chem.279 (46):48319–28.doi:10.1074/jbc.M404440200.PMID 15319445.
Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (2005)."Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer".Mol. Cell. Proteomics.4 (6):785–95.doi:10.1074/mcp.M500021-MCP200.PMID 15778465.
Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (2005). "A human protein–protein interaction network: a resource for annotating the proteome".Cell.122 (6):957–68.doi:10.1016/j.cell.2005.08.029.hdl:11858/00-001M-0000-0010-8592-0.PMID 16169070.S2CID 8235923.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein–protein interaction network".Nature.437 (7062):1173–8.Bibcode:2005Natur.437.1173R.doi:10.1038/nature04209.PMID 16189514.S2CID 4427026.
Göransson O, Deak M, Wullschleger S, Morrice NA, Prescott AR, Alessi DR (2007). "Regulation of the polarity kinases PAR-1/MARK by 14-3-3 interaction and phosphorylation".J. Cell Sci.119 (Pt 19):4059–70.doi:10.1242/jcs.03097.PMID 16968750.S2CID 582486.
Dequiedt F, Martin M, Von Blume J, Vertommen D, Lecomte E, Mari N, Heinen MF, Bachmann M, Twizere JC, Huang MC, Rider MH, Piwnica-Worms H, Seufferlein T, Kettmann R (2006)."New role for hPar-1 kinases EMK and C-TAK1 in regulating localization and activity of class IIa histone deacetylases"(PDF).Mol. Cell. Biol.26 (19):7086–102.doi:10.1128/MCB.00231-06.PMC 1592903.PMID 16980613.
Wissing J, Jänsch L, Nimtz M, Dieterich G, Hornberger R, Kéri G, Wehland J, Daub H (2007)."Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry".Mol. Cell. Proteomics.6 (3):537–47.doi:10.1074/mcp.T600062-MCP200.hdl:10033/19756.PMID 17192257.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007)."Large-scale mapping of human protein–protein interactions by mass spectrometry".Mol. Syst. Biol.3 (1): 89.doi:10.1038/msb4100134.PMC 1847948.PMID 17353931.

v t e PDB gallery
1ul7: Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3

Kinases:Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated mTOR EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1
Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3 PDK4
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4
Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase Aurora C kinase
Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-
IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP
cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY
cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1
Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3
Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase
Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2
G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6
Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK1A CAMK1B CAMK1D CAMK1G CAMK2 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1
Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4
Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2
Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19
Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4
Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1
Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14
MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14
Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-
Tropomyosin kinase (EC 2.7.11.28)	-
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-
Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

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